ArticleThe Journal of biological chemistry2018
A motif in HSP90 and P23 that links molecular chaperones to efficient estrogen receptor α methylation by the lysine methyltransferase SMYD2.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- Engineering a Membrane-Anchored CreER Recombinase With Reduced Basal Activity for In Vitro Recombination.Biotechnology journal · 2026Article
- Role of SMYD2 in gastrointestinal cancer progression (Review).Oncology letters · 2025Review
- PTGES3 proteolysis using the liposomal peptide-PROTAC approach.Biology direct · 2024Article
- Lysine and arginine methylation of transcription factors.Cellular and molecular life sciences : CMLS · 2024Review
- HSP90 mediates the connection of multiple programmed cell death in diseases.Cell death & disease · 2022Review
- Comparative transcriptome analysis of heat-induced domesticated zebrafish during gonadal differentiation.BMC genomic data · 2022Article
- How Protein Methylation Regulates Steroid Receptor Function.Endocrine reviews · 2022Review
- Protein expression profiling of rat uteruses with primary dysmenorrhea syndrome.Archives of gynecology and obstetrics · 2022Article
- An immune epigenetic insight to COVID-19 infection.Epigenomics · 2021Review
- SNP ofJournal of genetics · 2020Article
- Heat-shock proteins: chaperoning DNA repair.Oncogene · 2020Review
- Histone methyltransferase SMYD2: ubiquitous regulator of disease.Clinical epigenetics · 2019Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat shock protein 90 (HSP90) is a molecular chaperone that supervises folding of cellular signaling proteins such as steroid receptors and many protein kinases. HSP90 relies on ATP hydrolysis for powering a conformational circuit that helps fold the client protein. To that end, HSP90 binds to co-chaperone proteins that regulate ATP hydrolysis rate or interaction with client proteins. Co-chaperones such as P23, cell division cycle 37 (CDC37), or activator of HSP90 ATPase activity 1 (AHA1) interact with the N-terminal or middle domain of HSP90, whereas others, such as HSP70/HSP90-organizing protein (HOP), use tetratricopeptide repeat (TPR) domains to bind the EEVD motif at the very C-terminal end of HSP90. Recently, the lysine methyltransferase SET and MYND domain-containing 2 (SMYD2) has been proposed as an HSP90-binding partner, and interaction analyses indicate that SMYD2 binding to HSP90 is independent of the EEVD motif. Using the amplified luminescence proximity homogeneous assay (Alpha) technique, I identified a new (M/I/L/V)P
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.